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Pharmacological characterization and region‐specific expression in brain of the β2‐ and β3‐subunits of the rat GABA A receptor
Author(s) -
Lolait Stephen J.,
O'Carroll Anne-Marie,
Kusano Kiyoshi,
Mahan Lawrence C.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81605-9
Subject(s) - interleukin 10 receptor, alpha subunit , protein subunit , interleukin 5 receptor alpha subunit , gabaa receptor , complementary dna , biology , gamma aminobutyric acid receptor subunit alpha 1 , interleukin 12 receptor, beta 1 subunit , microbiology and biotechnology , cys loop receptors , xenopus , receptor , g alpha subunit , gabaa rho receptor , beta (programming language) , in situ hybridization , cdna library , messenger rna , biochemistry , gene , nicotinic agonist , nicotinic acetylcholine receptor , computer science , programming language
The cDNA for a third β‐subunit of the rat GABA a receptor has been cloned using another β‐subunit, which we had previously cloned [(1989) FEBS Lett. 246, 145‐148], as a probe. The ~ 8‐kb cDNA for this β‐subunit (termed β2) encodes a protein of 474 amino acid residues that shares ~ 80% sequence identity with the rat and bovine β1‐ and β3‐subunits. Coexpression of the cloned β‐subunit cDNA with the α1‐subunit cDNA of the rat GABA a receptor in Xenopus oocytes produced a functional receptor and Cl − channel with pharmacological characteristics of a GABA a receptor. In contrast to interchanging α‐subunits [(1988) Nature 335, 76‐79], exchange of β2‐ or β3‐subunits in α1/β receptor complex did not markedly alter the pharmacological properties of expressed receptors. In situ hybridization histochemistry with synthetic subunit‐specific oligodeoxynucleotide probes revealed a region‐specific expression of α1‐, β2‐ and β3‐subunit mRNAs in the rat central nervous system. These observations provide an additional molecular basis for the functional heterogeneity in the GABA A receptor complex.